Abstract
How force development and time under tension (TUT) during resistance exercise (RE) influence anabolic signalling of skeletal muscle is incompletely understood. We hypothesized that high force development during RE is more important for post-exercise-induced signalling than submaximal and fatiguing RE with lower force development but similar TUT. Twenty-two male subjects (24 ± 6 years, 181 ± 9 cm, 79 ± 2 kg) performed three distinct RE modes in the fed state with equal TUT but distinct force output: (i) maximal eccentric RE (ECC, n = 7) three sets, eight reps, 100 % eccentric dynamic force; (ii) standard RE (STD, n = 7), three sets, 10 reps, 75 % dynamic force; and (iii) high fatiguing single-set RE (HIT, n = 8), 20 reps, 100 % eccentric-concentric force; vastus lateralis biopsies were collected at baseline, 15, 30, 60, 240 min and 24 h after RE, and the signalling of mechanosensitive and mammalian target of rapamycin (mTOR)-related proteins was determined. The phosphorylation levels of pFAKTyr397, pJNKThr183/Tyr185, pAKTThr308/Ser473, pmTORSer2448, p4E-BP1Thr37/46, p70s6kThr389/Ser421/Thr424 and pS6Ser235/236 were significantly higher in ECC than those in STD and HIT at several time points (P < 0.01). pJNKThr183/Tyr185 and pS6Ser235/236 levels were significantly higher in type II myofibres in ECC compared with STD and HIT. HIT exerted throughout the weakest signalling response. We conclude that high force development during acute RE is superior for anabolic skeletal muscle signalling than fatiguing RE with lower force output but similar TUT. Our results suggest that this response is substantially driven by the higher activation of type II myofibres during RE.
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Abbreviations
- Nm:
-
Newton meter
- RE:
-
Resistance exercise
- REPS:
-
Repetitions
- TUT:
-
Time under tension
- AKT:
-
v-AKT murine thyoma viral oncogene
- 4E-BP1:
-
Eukaryotic initiation factor 4E-binding protein 1
- MAPK:
-
Mitogen-activated protein kinase
- mTOR:
-
Mammalian target of rapamycin
- JNK:
-
c-jun N-terminal kinase
- p70S6K:
-
70 kDa S6 protein kinase
- p90RSK:
-
90 kDa ribosomal S6 protein kinase
- S6:
-
S6 ribosomal protein
- FAK:
-
Focal adhesion kinase
- AMPK:
-
5-AMP-activated protein kinase
- GSK3-β:
-
Glycogen synthase kinase 3 beta
- TSC-2:
-
Tuberous sclerosis complex 2 (Tuberin)
- CK:
-
Creatine kinase
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Acknowledgments
The authors thank Katharina Hermanns and the technicians Anika Voss, Bianca Collins and Mojghan Ghilav (Institute of Cardiovascular Research and Sport Medicine, Department of Molecular and Cellular Sport Medicine) for expert technical assistance.
Conflict of interest
All authors disclose any professional relationship with companies or manufacturers who will benefit from the results of the present study.
Funding
This investigation was funded by the Federal Institute of Sports Science (BISP) IIA1-507 070103/09-10. The funders had no role in study design, data collection and analysis, decision to publish or preparation of the manuscript.
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Figure 7 Supplementary data
(A) Ratio of phosphorylated pGSK3-β Ser9to α-Tubulin and (B) pTSC-2Thr1462tototal levelsin STD, HIT and ECC. Ratios are from rested fed baseline conditions and 15, 30, 60, 240 min and 24 h after RE. Values are displayed as means ± S.E.M. Data are expressed in arbitrary units (AU). ∗Significantly different from PRE within each exercise group, P < 0.05. § Significantly different from STD within that time point, P < 0.05. # Significantly different from HIT within that time point, P < 0.05. + significantly different between HIT and STD within that time point, P < 0.05. (GIF 63 kb)
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Gehlert, S., Suhr, F., Gutsche, K. et al. High force development augments skeletal muscle signalling in resistance exercise modes equalized for time under tension. Pflugers Arch - Eur J Physiol 467, 1343–1356 (2015). https://doi.org/10.1007/s00424-014-1579-y
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DOI: https://doi.org/10.1007/s00424-014-1579-y